NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid-binding protein.
about
Bile acid binding protein: a versatile host of small hydrophobic ligands for applications in the fields of MRI contrast agents and bio-nanomaterialsA single amino acid mutation in zebrafish (Danio rerio) liver bile acid-binding protein can change the stoichiometry of ligand bindingStructural Requirements for Cooperativity in Ileal Bile Acid-binding ProteinsA disulfide bridge allows for site-selective binding in liver bile acid binding protein thereby stabilising the orientation of key amino acid side chainsStructural determinants of ligand binding in the ternary complex of human ileal bile acid binding protein with glycocholate and glycochenodeoxycholate obtained from solution NMRNMR studies of the dynamics of high-spin nitrophorins: comparative studies of NP4 and NP2 at close to physiological pHNMR studies of the dynamics of nitrophorin 2 bound to nitric oxide.NMR investigation of the equilibrium partitioning of a water-soluble bile salt protein carrier to phospholipid vesicles.The change of protein intradomain mobility on ligand binding: is it a commonly observed phenomenon?Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulationThe second transmembrane domain of the large conductance, voltage- and calcium-gated potassium channel beta(1) subunit is a lithocholate sensor.Bile salt recognition by human liver fatty acid binding protein.Disulfide bridge regulates ligand-binding site selectivity in liver bile acid-binding proteins.Chicken ileal bile-acid-binding protein: a promising target of investigation to understand binding co-operativity across the protein family.High relaxivity supramolecular adducts between human-liver fatty-acid-binding protein and amphiphilic Gd(III) complexes: structural basis for the design of intracellular targeting MRI probes.Wards in the keyway: amino acids with anomalous pK(a)s in calycins.Structural insight into a partially unfolded state preceding aggregation in an intracellular lipid-binding protein.
P2860
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P2860
NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid-binding protein.
description
2006 nî lūn-bûn
@nan
2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
NMR dynamic studies suggest th ...... ver bile acid-binding protein.
@ast
NMR dynamic studies suggest th ...... ver bile acid-binding protein.
@en
type
label
NMR dynamic studies suggest th ...... ver bile acid-binding protein.
@ast
NMR dynamic studies suggest th ...... ver bile acid-binding protein.
@en
prefLabel
NMR dynamic studies suggest th ...... ver bile acid-binding protein.
@ast
NMR dynamic studies suggest th ...... ver bile acid-binding protein.
@en
P2093
P2860
P356
P1476
NMR dynamic studies suggest th ...... ver bile acid-binding protein.
@en
P2093
Daniel Cicero
Henriette Molinari
Jefferson Foote
Laura Ragona
Lucia Zetta
Maddalena Catalano
Marianna Luppi
Tommaso Eliseo
P2860
P304
P356
10.1074/JBC.M513003200
P407
P577
2006-01-26T00:00:00Z